Nitrile Hydratase from Rhodococcus rhodochrous J1 Contains a Non-Corrin Cobalt Ion with Two Sulfur Ligands

We present spectroscopic data that show that a nitrile hydratase from Rhodococcus rhodochrous J1 is the first reported example of a native protein that contains a non-corrin Co super(3+) ion with a mixed S and N(O) ligand field. Two cobalt-containing nitrile hydratases have been identified in R. rho...

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Bibliographic Details
Published in:Journal of the American Chemical Society 1996-09, Vol.118 (38), p.9194-9195
Main Authors: Brennan, Bridget A, Alms, Geoffrey, Nelson, Mark J, Durney, Lewellyn T, Scarrow, Robert C
Format: Article
Language:English
Subjects:
Rhodococcus rhodochrous
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Summary:We present spectroscopic data that show that a nitrile hydratase from Rhodococcus rhodochrous J1 is the first reported example of a native protein that contains a non-corrin Co super(3+) ion with a mixed S and N(O) ligand field. Two cobalt-containing nitrile hydratases have been identified in R. rhodochrous J1. We purified one of those enzymes a multimer of alpha beta heterodimers totaling approximately 500 000 Da and containing non-corrin Co super(3+). We measured the cobalt super(12) and the protein super(13) concentrations of samples of purified enzyme and found one cobalt ion per ( alpha beta ). The same experiment yielded an unusually high epsilon 280 (2.7 (mg/mL) super(-1) cm super(-1)), consistent with an earlier report. super(10) EPR spectra of concentrated samples (0.3 mM cobalt) showed no signals attributable to the protein from 4 to 77 K, consistent with the presence of Co super(3+).
ISSN:0002-7863
1520-5126
DOI:10.1021/ja961920d